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Concerning the enigmatic cytochrome b-559 of oxygenic photosynthesis

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Abstract

Although there is an extensive literature on the properties and possible electron transfer pathways of cytochrome b-559, which is a prominent subunit of the multi-subunit photosystem II complex which functions in oxygenic photosynthesis, there is presently no consensus on the function of b-559 in the photosynthetic electron transport chain. The inability in earlier times to define a redox-linked function of this cytochrome was, to a large extent, a consequence of an absence of biochemical and structure information to complement an extensive array of spectrophotometric studies of the cytochrome in situ. Based on the location of hetero-dimeric b-559 in the photosystem II reaction center complex, derived from crystal crystallographic structure analysis, and the absence of a necessary redox function for the cytochrome in PSII, it is proposed that the main function of cytochrome b-559 is linked to its role as a structure component in the PSII reaction center complex. This function resides in the association of b-559 through its heme histidine residues in the trans-membrane domains of the PsbE and PsbF subunits of the PSII reaction center. These subunits, along with PsbJ, are inferred, from the analysis of structure, to define the intra-membrane portal in the PSII reaction center for plastoquinol (PQH2) export which, through the PSII complex, provides the redox link to the cytochrome b6f complex in the electron transfer chain.

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Abbreviations

ATP:

Adenosine; cyt, cytochrome

mDa:

Megadalton

ms:

Millisecond

OEC:

Oxygen-evolving complex

PQ:

Plastoquinone

p, n :

Electrochemically positive and negative sides of the membrane

PS:

Photosystem

Psb:

An acronym for photosystem II

References

  • Babcock GT, Widger WR, Cramer WA, Oertling WA, Metz JG (1985) Axial ligands of cytochrome b-559: identification and requirement for a heme-cross-linked polypeptide structure. Biochemistry 24:3638–3645

    Article  CAS  Google Scholar 

  • Boardman NK, Anderson J (1967) Fractionation of the photochemical systems of photosynthesis. II. cytochrome and carotenoid contents of particles isolated from spinach chloroplasts. Biochim Biophys Acta 143:187–203

    Article  CAS  Google Scholar 

  • Böhme H, Cramer WA (1971) Plastoquinone mediates electron transport between cytochrome b-559 and cytochrome f in spinach chloroplasts. FEBS Lett 15:349–435

    Article  Google Scholar 

  • Chance B (1982) Structure and function of the redox site of cytochrome oxidase. Adv Exp Med Biol 148:95–109

    Article  CAS  Google Scholar 

  • Chu H-A, Chen Y-H (2016) The roles of cytochrome b-559 in assembly and photoprotection of photosystem II revealed by site-directed mutagenesis studies. Front Plant Sci 6:1261

    Article  Google Scholar 

  • Cramer WA, Butler WL (1967) Light induced absorption changes of twocytochrome b components in the electron transport chain of spinach chloroplasts. Biochim Biophys Acta 14:332–339

    Article  Google Scholar 

  • Cramer, W. A., and D. B. Knaff (1991) Oxidation-Reduction; Electron and Proton Transfer. Energy Transduction in Biological Membranes; Chapter 2; Springer Study Edition [paperback, ISBN 0–387–97533–0]; 579 pp.

  • Cramer WA, Tae G-S, Furbacher P, Bottger M (1993) The enigmatic cytochrome b-559 of oxygenic photosynthesis. Physiol Plant 88:705–711

    Article  CAS  Google Scholar 

  • Crofts AR, Berry EA (1998) Structure and function of the cytochrome bc1 complex of mitochondria and photosynthetic bacteria. Curr Opin Struct Biol 8:501–509

    Article  CAS  Google Scholar 

  • Deisenhofer J, Michel H (1989) The photosynthetic reaction center from the purple photosynthetic bacterium, Rhodopseudomonas viridis. Science 245:1463–1473

    Article  CAS  Google Scholar 

  • Van Eerden FJ, Melo MN, Frederix PWJM, Periole X, Marrink SJ (2017) Exchange pathways of plastoquinone and plastoquinol in the photosystem II complex. Nature Comm 8:15214–15221

    Article  Google Scholar 

  • Horton P, Cramer WA (1974) The accessibility of the chloroplast cytochromes f and b-559 to ferricyanide. Biochim Biophys Acta 368:348–360

    Article  CAS  Google Scholar 

  • Horton P, Cramer WA (1975) Acid-base induced redox changes of the chloroplast b-559. FEBS Lett 56:244–247

    Article  CAS  Google Scholar 

  • Horton P, Whitmarsh J, Cramer WA (1976) On the specific site of action of 3-(3,4 di-chlorophenyl)-1,1-dimethylurea in chloroplasts: Inhibition of a dark acid-induced decrease in midpoint potential of cytochrome b-559. Arch Biochem Biophys 17:519–524

    Article  Google Scholar 

  • Kaminskaya O, Shuvalov VA, Renger G (2007) Evidence for a novel quinone binding site in the photosystem II (PS II) complex that regulates the redox potential of cytochrome b559. Biochemistry 46:1091–1105

    Article  CAS  Google Scholar 

  • Kern J et al (2018) Structures of the intermediates of Kok’s photosynthetic water oxidation clock. Nature 563:421–425

    Article  CAS  Google Scholar 

  • Knaff DB, Arnon DI (1969) Light-induced photo-oxidation of a chloroplast b-type cytochrome at -189 C. Proc. Natl Acad Sci. U S 63:956–962

    Article  CAS  Google Scholar 

  • Lundegarth H (1962) Quantitative relations between chlorophyll and cytochromes in chloroplasts. Physiol Plantarum 15:390

    Article  Google Scholar 

  • McKenzie SD, Ibrahim IM, Aryal UK, Puthiyaveetil S (2020) Stoichiometry of protein complexes in plant photosynthetic membranes. Biochim Biophys Acta 2:148141

    Article  Google Scholar 

  • Müh F, Zouni A (2016) Cytochrome b559 in Photosystem II. In: Cramer WA, Kallas T (eds) Cytochrome complexes, evolution, structures, energy transduction, and signaling advances in photosynthesis and respiration, vol 41. Springer, Dordrecht, pp 143–175

    Google Scholar 

  • Pakrasi HB, De Ciechi P, Whitmarsh J (1991) Site directed mutagenesis of the heme axial ligands of cytochrome b559 affects the stability of the photosystem II complex. The EMBO J 10:1619–1627

    Article  CAS  Google Scholar 

  • Pospisil P (2011) Enzymatic function of cytochrome b-559 in photosystem II. Photochem Photobiol B 104:141–147

    Article  Google Scholar 

  • Slater EC (1967) An evaluation of the Mitchell hypothesis of chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Eur J Biochem 1:317–326

    Article  CAS  Google Scholar 

  • Tae G-S, Everly RM, Cramer WA, Madgwick SA, Rich PR (1993) On the question of the identity of cytochrome b-560 in thylakoid stromal membranes. Photosyn Res 36:141–146

    Article  CAS  Google Scholar 

  • Thompson LK, Brudvig GW (1988) Cytochrome b-559 may function to protect photosystem II from photoinhibition. Biochemistry 27:6653–6658

    Article  CAS  Google Scholar 

  • Whitmarsh J, Cramer WA (1978) A pathway for the reduction of cytochrome b-559 by photosystem II in chloroplasts. Biochim Biophys Acta 501:83–93

    Article  CAS  Google Scholar 

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Acknowledgements

The authors’ research on ‘Structure-Function of Cytochromes in Oxygenic Photosynthesis,’ was supported at different times by non-overlapping grants from the Fogarty Foundation (TW0-1235), the National Science Foundation (GB-26635), the National Institutes of Health (GM-18457), a Research Career Development Award from the NIH (1 KO4 GM-29735), and grants from the USDA (59-2182-1-1-683-0) and DOE (Dept. of Energy) grant DE-SC0018238. We thank R. Harding for assistance with the assembly of the manuscript.

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Cramer, W.A., Zakharov, S.D. Concerning the enigmatic cytochrome b-559 of oxygenic photosynthesis. Photosynth Res 153, 157–162 (2022). https://doi.org/10.1007/s11120-022-00936-5

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